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TitleStructure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 23, Page e2424678122, Year 2025
Publish dateJun 10, 2025
AuthorsMonica Gonzalez-Magaldi / Anuradha Gullapalli / Ophelia Papoulas / Chang Liu / Adelaide Y-H Leung / Luqiang Guo / Axel F Brilot / Edward M Marcotte / Zunlong Ke / Daniel J Leahy /
PubMed AbstractWe report here transport of full-length epidermal growth factor receptor (EGFR), Insulin Receptor, 7-pass transmembrane receptor Smoothened, and 13-pass Sodium-iodide symporter to extracellular ...We report here transport of full-length epidermal growth factor receptor (EGFR), Insulin Receptor, 7-pass transmembrane receptor Smoothened, and 13-pass Sodium-iodide symporter to extracellular vesicles (EVs) for structural and functional studies. Mass spectrometry confirmed the transported proteins are the most abundant in EV membranes, and the presence of many receptor-interacting proteins in EVs demonstrates their utility for characterizing membrane protein interactomes. Cryo-electron tomography of EGFR-containing EVs reveals that EGFR forms clusters in both the presence and absence of EGF with a ~3 nm gap between the inner membrane and cytoplasmic density. EGFR extracellular region (ECR) dimers do not form regular arrays in these clusters. Subtomogram averaging of the 150 kDa EGF-bound EGFR ECR dimer yielded a 15 Å map into which the crystal structure of the ligand-bound EGFR ECR dimer fits well. These findings refine our understanding of EGFR activation, clustering, and signaling and establish EVs as a versatile platform for structural and functional characterization of human membrane proteins in cell-derived membranes.
External linksProc Natl Acad Sci U S A / PubMed:40455995 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution15.0 Å
Structure data

EMDB-49404: Subtomogram Averaging of Liganded EGFR Dimer from Extracellular Vesicle
Method: EM (subtomogram averaging) / Resolution: 15.0 Å

Source
  • Homo sapiens (human)

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